FTSZ_STRP2
ID FTSZ_STRP2 Reviewed; 419 AA.
AC A0A0H2ZNE0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=SPD_1479;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=28941257; DOI=10.1111/mmi.13847;
RA Zheng J.J., Perez A.J., Tsui H.T., Massidda O., Winkler M.E.;
RT "Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses
RT the requirement for PBP2b by overproduction of FtsA in Streptococcus
RT pneumoniae D39.";
RL Mol. Microbiol. 106:793-814(2017).
CC -!- FUNCTION: Essential cell division protein that forms a contractile ring
CC structure (Z ring) at the future cell division site. The regulation of
CC the ring assembly controls the timing and the location of cell
CC division. One of the functions of the FtsZ ring is to recruit other
CC cell division proteins to the septum to produce a new cell wall between
CC the dividing cells. Binds GTP and shows GTPase activity.
CC {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC strictly GTP-dependent manner. Interacts directly with several other
CC division proteins. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- INDUCTION: Protein level is negatively regulated by KhpA/KhpB at the
CC transcriptional level (at protein level).
CC {ECO:0000269|PubMed:28941257}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; CP000410; ABJ54579.1; -; Genomic_DNA.
DR RefSeq; WP_000144280.1; NC_008533.2.
DR SMR; A0A0H2ZNE0; -.
DR STRING; 373153.SPD_1479; -.
DR EnsemblBacteria; ABJ54579; ABJ54579; SPD_1479.
DR GeneID; 60234481; -.
DR KEGG; spd:SPD_1479; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_1_2_9; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR BioCyc; SPNE373153:G1G6V-1595-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-UniRule.
DR CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR HAMAP; MF_00909; FtsZ; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF12327; FtsZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR TIGRFAMs; TIGR00065; ftsZ; 1.
DR PROSITE; PS01134; FTSZ_1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Septation.
FT CHAIN 1..419
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000454547"
FT REGION 397..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 109..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ SEQUENCE 419 AA; 44416 MW; EEBB217812BD2B90 CRC64;
MTFSFDTAAA QGAVIKVIGV GGGGGNAINR MVDEGVTGVE FIAANTDVQA LSSTKAETVI
QLGPKLTRGL GAGGQPEVGR KAAEESEETL TEAISGADMV FITAGMGGGS GTGAAPVIAR
IAKDLGALTV GVVTRPFGFE GSKRGQFAVE GINQLREHVD TLLIISNNNL LEIVDKKTPL
LEALSEADNV LRQGVQGITD LITNPGLINL DFADVKTVMA NKGNALMGIG IGSGEERVVE
AARKAIYSPL LETTIDGAED VIVNVTGGLD LTLIEAEEAS QIVNQAAGQG VNIWLGTSID
ESMRDEIRVT VVATGVRQDR VEKVVAPQAR SATNYRETVK PAHSHGFDRH FDMAETVELP
KQNPRRLEPT QASAFGDWDL RRESIVRTTD SVVSPVERFE APISQDEDEL DTPPFFKNR
